The peroxidase has been commonly used in many biotechnology fields but such potentially applications are limited because peroxidase loses activity with a mechanism-based (suicide) mode. Our study elucidated that the formation of a covalent bond between Corprinus cinereus peroxydase (CiP) and the phenol could be a major factor in the inactivation of CiP. Mass spectrometry analysis of inactivated CiP revealed that amino residue F229 was modified by phenol through phenol oxidation reaction. Among F229-mutant CiP, F229A led to a peroxidase with 70 times the residual activity and showed 14-fold higher turnover capacity than that of wild-type. As a modeling result, removal of F229 residue at the entrance of the enzyme led to greater resistance against phenoxyl radical interaction. The lower HOMO energy and binding free energy of F229A with phenol supported this result. Therefore, F229-mutant CiP has the radical-resistant and can be efficiently used in the polymerization of various phenolics.

Development of the radical-robust <i>Coprinus cinereus</i> peroxidase by blocking suicide pathway to improve the polymerization of phenolics

241st National Meeting (2011)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.

Development of the radical-robust Coprinus cinereus peroxidase by blocking suicide pathway to improve the polymerization of phenolics